Gel filtration chromatography as a versatile tool in lectin purification - A review
TL;DR
The role of gel filtration chromatography as a gentle, size-based technique for purifying lectins from diverse biological sources while preserving their structural integrity and bioactivity is comprehensively summarized.
Abstract
Lectins are a diverse class of carbohydrate-binding proteins found throughout nature, known for their significant biological and therapeutic potential. They play crucial roles in immune modulation, pathogen recognition, antiviral defense, and cancer inhibition. Due to their biomedical importance, the purification of lectins in a pure and structurally intact form is essential for precise structural and functional studies. Among various purification methods, gel filtration chromatography (GFC) has proven to be a reliable and gentle technique for separating lectins according to molecular size while preserving their natural conformation and bioactivity. This review summarizes the use of GFC for lectin purification from diverse sources such as plants, fungi, algae, animals, and microorganisms. GFC effectively distinguishes monomeric, dimeric, and multimeric lectins, offering insights into their molecular weight, structural integrity, and homogeneity. Although the method maintains protein activity and compatibility with downstream analyses, it shows limited resolution for proteins of similar molecular size, often requiring additional purification steps. Overall, GFC remains a fundamental and versatile technique in lectin purification, contributing substantially to advancements in analytical chemistry, glycoscience, immunology, and pharmaceutical research. This review comprehensively summarizes the role of gel filtration chromatography as a gentle, size-based technique for purifying lectins from diverse biological sources while preserving their structural integrity and bioactivity.